KI11B_XENLA
ID KI11B_XENLA Reviewed; 1067 AA.
AC P28025;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Kinesin-like protein KIF11-B;
DE AltName: Full=Kinesin-5;
DE AltName: Full=Kinesin-related motor protein Eg5-1;
DE Short=XLEg5K1;
DE Short=XlEg5;
GN Name=kif11-b; Synonyms=eg5;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Egg;
RX PubMed=1710028; DOI=10.1128/mcb.11.6.3395-3398.1991;
RA le Guellec R., Paris J., Couturier A., Roghi C., Philippe M.;
RT "Cloning by differential screening of a Xenopus cDNA that encodes a
RT kinesin-related protein.";
RL Mol. Cell. Biol. 11:3395-3398(1991).
RN [2]
RP INTERACTION WITH AURKA, SUBCELLULAR LOCATION, AND SERINE PHOSPHORYLATION.
RX PubMed=10329703; DOI=10.1074/jbc.274.21.15005;
RA Giet R., Uzbekov R., Cubizolles F., Le Guellec K., Prigent C.;
RT "The Xenopus laevis aurora-related protein kinase pEg2 associates with and
RT phosphorylates the kinesin-related protein XlEg5.";
RL J. Biol. Chem. 274:15005-15013(1999).
RN [3]
RP FUNCTION.
RX PubMed=15583027; DOI=10.1083/jcb.200407126;
RA Miyamoto D.T., Perlman Z.E., Burbank K.S., Groen A.C., Mitchison T.J.;
RT "The kinesin Eg5 drives poleward microtubule flux in Xenopus laevis egg
RT extract spindles.";
RL J. Cell Biol. 167:813-818(2004).
RN [4]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-1046.
RX PubMed=19001501; DOI=10.1242/jcs.035360;
RA Rapley J., Nicolas M., Groen A., Regue L., Bertran M.T., Caelles C.,
RA Avruch J., Roig J.;
RT "The NIMA-family kinase Nek6 phosphorylates the kinesin Eg5 at a novel site
RT necessary for mitotic spindle formation.";
RL J. Cell Sci. 121:3912-3921(2008).
RN [5]
RP PHOSPHORYLATION AT THR-937, AND MUTAGENESIS OF THR-937.
RX PubMed=19079595; DOI=10.1371/journal.pone.0003936;
RA Cahu J., Olichon A., Hentrich C., Schek H., Drinjakovic J., Zhang C.,
RA Doherty-Kirby A., Lajoie G., Surrey T.;
RT "Phosphorylation by Cdk1 increases the binding of Eg5 to microtubules in
RT vitro and in Xenopus egg extract spindles.";
RL PLoS ONE 3:E3936-E3936(2008).
CC -!- FUNCTION: Plus end-directed motor protein required for establishing a
CC bipolar spindle (PubMed:15583027). Associates with both interphase and
CC spindle microtubules (PubMed:15583027). May be involved in nuclear
CC divisions taking place during the development of unfertilized eggs
CC (PubMed:15583027). Required in non-mitotic cells for transport of
CC secretory proteins from the Golgi complex to the cell surface (By
CC similarity). {ECO:0000250|UniProtKB:P52732,
CC ECO:0000269|PubMed:15583027}.
CC -!- SUBUNIT: Heterotetramer of two heavy and two light chains. Interacts
CC with aurka. {ECO:0000269|PubMed:10329703}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, spindle pole.
CC Note=Concentrated around the polar ends of both meiotic and mitotic
CC spindles.
CC -!- TISSUE SPECIFICITY: In unfertilized eggs, shows highest expression in
CC the germinal vesicle and radial yolk-poor channels. Also present in
CC testis. {ECO:0000269|PubMed:1710028}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally. Expressed in eggs but not
CC oocytes (at protein level). The RNA is subject to translational control
CC and is only adenylated in eggs. Expression stops soon after
CC fertilization, when the mRNA is deadenylated. Not expressed in adults.
CC {ECO:0000269|PubMed:1710028}.
CC -!- PTM: Phosphorylation of Thr-937 during mitosis controls the association
CC of this protein with the spindle apparatus.
CC {ECO:0000269|PubMed:19001501, ECO:0000269|PubMed:19079595}.
CC -!- PTM: A subset of this protein primarily localized at the spindle pole
CC is phosphorylated by NEK6 during mitosis.
CC -!- PTM: Phosphorylated on a serine residue by aurka.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. BimC subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA37950.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X54002; CAA37950.1; ALT_INIT; mRNA.
DR PIR; A40264; A40264.
DR RefSeq; NP_001095237.1; NM_001101767.1.
DR AlphaFoldDB; P28025; -.
DR SMR; P28025; -.
DR IntAct; P28025; 1.
DR iPTMnet; P28025; -.
DR PRIDE; P28025; -.
DR GeneID; 397908; -.
DR KEGG; xla:397908; -.
DR CTD; 397908; -.
DR Xenbase; XB-GENE-6252175; kif11.S.
DR OrthoDB; 179272at2759; -.
DR Proteomes; UP000186698; Chromosome 7S.
DR Bgee; 397908; Expressed in egg cell and 17 other tissues.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0003777; F:microtubule motor activity; IMP:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR025901; Kinesin-assoc_MT-bd_dom.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF13931; Microtub_bind; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Mitosis; Motor protein; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1067
FT /note="Kinesin-like protein KIF11-B"
FT /id="PRO_0000125373"
FT DOMAIN 18..359
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT COILED 365..480
FT /evidence="ECO:0000255"
FT BINDING 105..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 937
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:19079595"
FT MOD_RES 1046
FT /note="Phosphoserine; by NEK6"
FT /evidence="ECO:0000269|PubMed:19001501"
FT MUTAGEN 937
FT /note="T->A: Disrupts microtubule binding."
FT /evidence="ECO:0000269|PubMed:19079595"
SQ SEQUENCE 1067 AA; 120114 MW; 051F664EF6BBE0E5 CRC64;
MSSQNSFMAS KKEDKGKNIQ VVVRCRPFNQ LERKASSHSV LECDSQRKEV YVRTGEVNDK
LGKKTYTFDM VFGPAAKQIE VYRSVVCPIL DEVIMGYNCT IFAYGQTGTG KTFTMEGERS
SDEEFTWEQD PLAGIIPRTL HQIFEKLSEN GTEFSVKVSL LEIYNEELFD LLSPSPDVGE
RLQMFDDPRN KRGVIIKGLE EISVHNKDEV YHILERGAAR RKTASTLMNA YSSRSHSVFS
VTIHMKETTV DGEELVKIGK LNLVDLAGSE NIGRSGAVDK RAREAGNINQ SLLTLGRVIT
ALVERTPHIP YRESKLTRIL QDSLGGRTKT SIIATVSPAS INLEETVSTL DYANRAKSIM
NKPEVNQKLT KKALIKEYTE EIERLKRELA AAREKNGVYL SSENYEQLQG KVLSQEEMIT
EYTEKITAME EELKSISELF ADNKKELEEC TTILQCKEKE LEETQNHLQE SKEQLAQESF
VVSAFETTEK KLHGTANKLL STVRETTRDV SGLHEKLDRK KAVDQHNFQV HENFAEQMDR
RFSVIQRTVD DYSVKQQGML DFYTNSIDDL LGASSSRLSA TASAVAKSFA SVQETVTKQV
SHSVEEILKQ ETLSSQAKGD LQQLMAAHRT GLEEALRSDL LPVVTAVLDL NSHLSHCLQN
FLIVADKIDS HKEDMNSFFT EHSRSLHKLR LDSSSALSSI QSEYESLKED IATAQSMHSE
GVNNLISSLQ NQLNLLGMET QQQFSGFLSK GGKLQKSVGS LQQDLDLVSS EAIECISSHH
KKLAEQSQDV AVEIRQLAGS NMSTLEESSK QCEKLTSSIN TISQESQQWC ESAGQKIDSV
LEEQVCYLHS SKKHLQNLHK GVEDSCGSSV VEITDRVNAQ RQAEEKALTS LVEQVRDDQE
MVGEQRLELQ EQVQSGLNKV HSYLKEELRN DVPTGTTPQR RDYAYPSLLV KTKPRDVLLE
QFRQQQQEYL ESISSVISEA VEPPVEQDSL EDEPPVAVND SVISERSCID LSMTCQEKGG
IRFFQQKKAL RKEKENRGNT TLLERSKIMD EVDQALTKSK LPLRMQN
